Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes.
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Embargo End Date
Authors
Abascal-Palacios, G
Jochem, L
Pla-Prats, C
Beuron, F
Vannini, A
Jochem, L
Pla-Prats, C
Beuron, F
Vannini, A
Document Type
Journal Article
Date
2021-11-30
Date Accepted
2021-11-15
Abstract
Retrotransposons are endogenous elements that have the ability to mobilise their DNA between different locations in the host genome. The Ty3 retrotransposon integrates with an exquisite specificity in a narrow window upstream of RNA Polymerase (Pol) III-transcribed genes, representing a paradigm for harmless targeted integration. Here we present the cryo-EM reconstruction at 4.0 Å of an active Ty3 strand transfer complex bound to TFIIIB transcription factor and a tRNA gene. The structure unravels the molecular mechanisms underlying Ty3 targeting specificity at Pol III-transcribed genes and sheds light into the architecture of retrotransposon machinery during integration. Ty3 intasome contacts a region of TBP, a subunit of TFIIIB, which is blocked by NC2 transcription regulator in RNA Pol II-transcribed genes. A newly-identified chromodomain on Ty3 integrase interacts with TFIIIB and the tRNA gene, defining with extreme precision the integration site position.
Citation
Nature communications, 2021, 12 (1), pp. 6992 - ?
Source Title
Publisher
NATURE PORTFOLIO
ISSN
2041-1723
eISSN
2041-1723
2041-1723
2041-1723
Collections
Research Team
Vannini Group
